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1Z5B

Topoisomerase VI-B, ADP AlF4- bound dimer form

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA binding
A0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
A0005524molecular_functionATP binding
A0006265biological_processDNA topological change
B0003676molecular_functionnucleic acid binding
B0003677molecular_functionDNA binding
B0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
B0005524molecular_functionATP binding
B0006265biological_processDNA topological change
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 2001
ChainResidue
AASN42
AADP1001
AALF3001
AHOH4038
AHOH4136

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ALF A 3001
ChainResidue
AGLY109
ALEU110
AGLY111
ALYS427
AADP1001
AMG2001
AHOH4002
AHOH4038
AHOH4136
AHOH4137
AGLU38
AGLY106
AMET107
ATYR108

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 2002
ChainResidue
BASN42
BADP1002
BALF3002
BHOH3008
BHOH3165

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ALF B 3002
ChainResidue
BGLU38
BGLY106
BMET107
BTYR108
BGLY109
BLEU110
BGLY111
BLYS427
BADP1002
BMG2002
BHOH3003
BHOH3008
BHOH3089
BHOH3165

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 4001
ChainResidue
AGLY266
AASP267
ATHR268
ATHR269
AARG307
AHOH4005
BARG307

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 2003
ChainResidue
BARG102
BTHR418
BHOH3030
BHOH3069

site_idAC7
Number of Residues26
DetailsBINDING SITE FOR RESIDUE ADP A 1001
ChainResidue
AASN42
AALA46
AASP76
AGLY80
AILE81
AALA89
ATYR95
ASER96
ASER97
ALYS98
AGLY106
AMET107
ATYR108
AGLY109
ALEU110
AGLY111
AVAL112
ALYS113
AMG2001
AALF3001
AHOH4004
AHOH4009
AHOH4011
AHOH4012
AHOH4136
BPHE7

site_idAC8
Number of Residues26
DetailsBINDING SITE FOR RESIDUE ADP B 1002
ChainResidue
BHOH3016
BHOH3165
APHE7
BASN42
BALA46
BASP76
BGLY80
BILE81
BALA89
BTYR95
BSER96
BSER97
BLYS98
BMET107
BTYR108
BGLY109
BLEU110
BGLY111
BVAL112
BLYS113
BTHR170
BMG2002
BALF3002
BHOH3007
BHOH3008
BHOH3010

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:12505993, ECO:0000269|PubMed:15939019, ECO:0007744|PDB:1MX0, ECO:0007744|PDB:1Z59, ECO:0007744|PDB:1Z5A, ECO:0007744|PDB:1Z5B, ECO:0007744|PDB:1Z5C
ChainResidueDetails
AASN42
AASP76
AMET107
BASN42
BASP76
BMET107

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12505993, ECO:0000269|PubMed:15939019, ECO:0007744|PDB:1MX0, ECO:0007744|PDB:1Z5A, ECO:0007744|PDB:1Z5B, ECO:0007744|PDB:1Z5C
ChainResidueDetails
ASER96
BSER96

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12505993, ECO:0007744|PDB:1MX0
ChainResidueDetails
ALYS427
BLYS427

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PDB entries from 2024-08-28

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